ID ECH1_HUMAN Reviewed; 328 AA. AC Q13011; A8K745; Q8WVX0; Q96EZ9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 2. DT 24-JAN-2024, entry version 212. DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial {ECO:0000305}; DE EC=5.3.3.- {ECO:0000250|UniProtKB:Q62651}; DE Flags: Precursor; GN Name=ECH1 {ECO:0000312|HGNC:HGNC:3149}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RX PubMed=7558027; DOI=10.1006/geno.1995.1077; RA Fitzpatrick D.R., Germain-Lee E., Valle D.; RT "Isolation and characterization of rat and human cDNAs encoding a novel RT putative peroxisomal enoyl-CoA hydratase."; RL Genomics 27:457-466(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Fitzpatrick D.R., Valle D.; RT "Genomic structure of human ECH1."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-41. RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-41. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-41. RC TISSUE=Melanoma, and Pancreatic carcinoma; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 149-158 AND 215-230, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 66-77; 113-131; 149-211; 215-230 AND 232-245, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, VARIANT [LARGE SCALE RP ANALYSIS] ALA-41, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 50-322. RG Structural genomics consortium (SGC); RT "Crystal structure of human peroxisomal delta3,5,delta2,4-dienoyl CoA RT isomerase (ECH1)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4- CC trans-dienoyl-CoA. {ECO:0000250|UniProtKB:Q62651}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(3E,5Z)-octadienoyl-CoA = (2E,4E)-octadienoyl-CoA; CC Xref=Rhea:RHEA:45244, ChEBI:CHEBI:62243, ChEBI:CHEBI:85108; CC Evidence={ECO:0000250|UniProtKB:Q62651}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3E,5Z,8Z,11Z,14Z)-eicosapentaenoyl-CoA = (2E,4E,8Z,11Z,14Z)- CC eicosapentaenoyl-CoA; Xref=Rhea:RHEA:45224, ChEBI:CHEBI:85090, CC ChEBI:CHEBI:85091; Evidence={ECO:0000250|UniProtKB:Q62651}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000250|UniProtKB:Q62651}. CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:Q62651}. CC -!- INTERACTION: CC Q13011; O75521: ECI2; NbExp=4; IntAct=EBI-711968, EBI-2512024; CC Q13011; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-711968, EBI-10175124; CC Q13011; P42858: HTT; NbExp=2; IntAct=EBI-711968, EBI-466029; CC Q13011; P40763: STAT3; NbExp=2; IntAct=EBI-711968, EBI-518675; CC Q13011; Q13077: TRAF1; NbExp=4; IntAct=EBI-711968, EBI-359224; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q62651}. CC Peroxisome {ECO:0000250|UniProtKB:Q62651}. CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U16660; AAC50222.1; -; mRNA. DR EMBL; AF030249; AAB86485.1; -; Genomic_DNA. DR EMBL; AF030246; AAB86485.1; JOINED; Genomic_DNA. DR EMBL; AF030247; AAB86485.1; JOINED; Genomic_DNA. DR EMBL; AF030248; AAB86485.1; JOINED; Genomic_DNA. DR EMBL; AK291860; BAF84549.1; -; mRNA. DR EMBL; CH471126; EAW56824.1; -; Genomic_DNA. DR EMBL; BC011792; AAH11792.1; -; mRNA. DR EMBL; BC017408; AAH17408.1; -; mRNA. DR CCDS; CCDS33014.1; -. DR PIR; I38882; I38882. DR RefSeq; NP_001389.2; NM_001398.2. DR PDB; 2VRE; X-ray; 1.95 A; A/B/C=50-322. DR PDBsum; 2VRE; -. DR AlphaFoldDB; Q13011; -. DR SMR; Q13011; -. DR BioGRID; 108220; 218. DR IntAct; Q13011; 200. DR MINT; Q13011; -. DR STRING; 9606.ENSP00000221418; -. DR ChEMBL; CHEMBL4523284; -. DR GlyGen; Q13011; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13011; -. DR MetOSite; Q13011; -. DR PhosphoSitePlus; Q13011; -. DR SwissPalm; Q13011; -. DR BioMuta; ECH1; -. DR DMDM; 82654933; -. DR REPRODUCTION-2DPAGE; IPI00011416; -. DR EPD; Q13011; -. DR jPOST; Q13011; -. DR MassIVE; Q13011; -. DR MaxQB; Q13011; -. DR PaxDb; 9606-ENSP00000221418; -. DR PeptideAtlas; Q13011; -. DR ProteomicsDB; 59100; -. DR Pumba; Q13011; -. DR TopDownProteomics; Q13011; -. DR Antibodypedia; 1042; 303 antibodies from 30 providers. DR DNASU; 1891; -. DR Ensembl; ENST00000221418.9; ENSP00000221418.3; ENSG00000104823.9. DR Ensembl; ENST00000634245.2; ENSP00000489530.1; ENSG00000282853.2. DR GeneID; 1891; -. DR KEGG; hsa:1891; -. DR MANE-Select; ENST00000221418.9; ENSP00000221418.3; NM_001398.3; NP_001389.2. DR UCSC; uc002oji.4; human. DR AGR; HGNC:3149; -. DR CTD; 1891; -. DR DisGeNET; 1891; -. DR GeneCards; ECH1; -. DR HGNC; HGNC:3149; ECH1. DR HPA; ENSG00000104823; Tissue enhanced (skeletal). DR MIM; 600696; gene. DR neXtProt; NX_Q13011; -. DR OpenTargets; ENSG00000104823; -. DR PharmGKB; PA27596; -. DR VEuPathDB; HostDB:ENSG00000104823; -. DR eggNOG; KOG1681; Eukaryota. DR GeneTree; ENSGT00940000159610; -. DR InParanoid; Q13011; -. DR OMA; QYVAHVE; -. DR OrthoDB; 553487at2759; -. DR PhylomeDB; Q13011; -. DR TreeFam; TF314317; -. DR PathwayCommons; Q13011; -. DR Reactome; R-HSA-9033241; Peroxisomal protein import. DR SignaLink; Q13011; -. DR UniPathway; UPA00659; -. DR BioGRID-ORCS; 1891; 15 hits in 1161 CRISPR screens. DR ChiTaRS; ECH1; human. DR EvolutionaryTrace; Q13011; -. DR GeneWiki; ECH1; -. DR GenomeRNAi; 1891; -. DR Pharos; Q13011; Tbio. DR PRO; PR:Q13011; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q13011; Protein. DR Bgee; ENSG00000104823; Expressed in apex of heart and 102 other cell types or tissues. DR ExpressionAtlas; Q13011; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome. DR GO; GO:0005777; C:peroxisome; NAS:UniProtKB. DR GO; GO:0051750; F:delta(3,5)-delta(2,4)-dienoyl-CoA isomerase activity; IBA:GO_Central. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR045002; Ech1-like. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR014748; Enoyl-CoA_hydra_C. DR PANTHER; PTHR43149:SF1; DELTA(3,5)-DELTA(2,4)-DIENOYL-COA ISOMERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43149; ENOYL-COA HYDRATASE; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. DR UCD-2DPAGE; Q13011; -. DR Genevisible; Q13011; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; KW Fatty acid metabolism; Isomerase; Lipid metabolism; Mitochondrion; KW Peroxisome; Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..33 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 34..328 FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, FT mitochondrial" FT /id="PRO_0000007417" FT MOTIF 326..328 FT /note="Microbody targeting signal" FT /evidence="ECO:0000255" FT BINDING 116..120 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P42126" FT BINDING 174 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P42126" FT SITE 197 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:P42126" FT SITE 205 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:Q62651" FT MOD_RES 231 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:O35459" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 327 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 41 FT /note="E -> A (in dbSNP:rs9419)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4, FT ECO:0007744|PubMed:24275569" FT /id="VAR_014927" FT VARIANT 217 FT /note="G -> R (in dbSNP:rs2229259)" FT /id="VAR_033913" FT CONFLICT 210 FT /note="Q -> E (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="R -> H (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT CONFLICT 239 FT /note="G -> D (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT CONFLICT 259 FT /note="A -> P (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="A -> P (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT CONFLICT 268..271 FT /note="SPVA -> TTVL (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="A -> P (in Ref. 1; AAC50222 and 2; AAB86485)" FT /evidence="ECO:0000305" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 64..72 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 75..77 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 83..97 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 120..128 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 135..158 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 169..172 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 174..179 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 208..215 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 219..228 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 234..239 FT /evidence="ECO:0007829|PDB:2VRE" FT STRAND 242..249 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 250..265 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 269..284 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 287..301 FT /evidence="ECO:0007829|PDB:2VRE" FT HELIX 305..313 FT /evidence="ECO:0007829|PDB:2VRE" SQ SEQUENCE 328 AA; 35816 MW; 211E0FF40379E6DA CRC64; MAAGIVASRR LRDLLTRRLT GSNYPGLSIS LRLTGSSAQE EASGVALGEA PDHSYESLRV TSAQKHVLHV QLNRPNKRNA MNKVFWREMV ECFNKISRDA DCRAVVISGA GKMFTAGIDL MDMASDILQP KGDDVARISW YLRDIITRYQ ETFNVIERCP KPVIAAVHGG CIGGGVDLVT ACDIRYCAQD AFFQVKEVDV GLAADVGTLQ RLPKVIGNQS LVNELAFTAR KMMADEALGS GLVSRVFPDK EVMLDAALAL AAEISSKSPV AVQSTKVNLL YSRDHSVAES LNYVASWNMS MLQTQDLVKS VQATTENKEL KTVTFSKL //